| CHEN, ling, Kelly TRUJILLO, Stephen VAN KOMEN, Dong ROH, Lumír KREJČÍ, Kevin LEWIS, Mike RESNICK, Patrick SUNG a Alan TOMKINSON. Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2005, roč. 280, č. 4, s. 2620-7, 7 s. ISSN 0021-9258. |
Další formáty:
BibTeX
LaTeX
RIS
@article{708606,
author = {Chen, ling and Trujillo, Kelly and Van Komen, Stephen and Roh, Dong and Krejčí, Lumír and Lewis, Kevin and Resnick, Mike and Sung, Patrick and Tomkinson, Alan},
article_location = {Bethesda, USA},
article_number = {4},
keywords = {Rad50; ATPase; repair;},
language = {eng},
issn = {0021-9258},
journal = {Journal of Biological Chemistry},
title = {Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15546877&query_hl=20&itool=pubmed_docsum},
volume = {280},
year = {2005}
}
TY - JOUR
ID - 708606
AU - Chen, ling - Trujillo, Kelly - Van Komen, Stephen - Roh, Dong - Krejčí, Lumír - Lewis, Kevin - Resnick, Mike - Sung, Patrick - Tomkinson, Alan
PY - 2005
TI - Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast.
JF - Journal of Biological Chemistry
VL - 280
IS - 4
SP - 2620-7
EP - 2620-7
PB - Amer. Soc. Biochem. Mol. Biol.
SN - 00219258
KW - Rad50
KW - ATPase
KW - repair;
UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15546877&query_hl=20&itool=pubmed_docsum
L2 - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15546877&query_hl=20&itool=pubmed_docsum
N2 - The Saccharomyces cerevisiae Rad50-Mre11-Xrs2 complex plays a central role in the cellular response to DNA double strand breaks. Rad50 has a globular ATPase head domain with a long coiled-coil tail. DNA binding by Rad50 is ATP-dependent and the Rad50-Mre11-Xrs2 complex possesses DNA unwinding and endonuclease activities that are regulated by ATP. Here we have examined the role of the Rad50 Walker type A ATP binding motif in DNA double strand break repair by a combination of genetic and biochemical approaches. Replacement of the conserved lysine residue within the Walker A motif with alanine, glutamate, or arginine results in the same DNA damage sensitivity and homologous recombination defect as the rad50 deletion mutation. The Walker A mutations also cause a deficiency in non-homologous end-joining. As expected, complexes containing the rad50 Walker A mutant proteins are defective in ATPase, ATP-dependent DNA unwinding, and ATP-stimulated endonuclease activities. Although the DNA end-bridging activity of the Rad50-Mre11-Xrs2 complex is ATP-independent, the end-bridging activity of complexes containing the rad50 Walker A mutant proteins is salt-sensitive. These results provide a molecular explanation for the observed in vivo defects of the rad50 Walker mutant strains and reveal a novel ATP-independent function for Rad50 in DNA end-bridging.
ER -
CHEN, ling, Kelly TRUJILLO, Stephen VAN KOMEN, Dong ROH, Lumír KREJČÍ, Kevin LEWIS, Mike RESNICK, Patrick SUNG a Alan TOMKINSON. Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2005, roč.~280, č.~4, s.~2620-7, 7 s. ISSN~0021-9258.
|
